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benzoyl-CoA substrate forms two hydrogen bonds with Gln116, which in turn is hydrogen-bonded to Glu120. A number of other second-shell residues are also important for the orientation of the benzoyl moiety, including Thr119, Ser123, Phe193, Phe203, and Thr210. Optimized structure of the BoxB active site with the truncated benzoyl-CoA and O2 substrates bound, corresponding to the Michaelis complex, enzyme structure and reaction mechanism mechanics/molecular mechanics calculations and modeling, overview
usage of PDB ID 3PM5 for enzyme structure modeling and simulation, quantum mechanics/molecular mechanics calculations, overview. Four general pathways for oxidizing aromatic rings are determined
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